LOCUS       AIG78772.1               456 aa    PRT              BCT 01-OCT-2014
DEFINITION  Amycolatopsis japonica Trigger factor protein.
ACCESSION   CP008953-5831
PROTEIN_ID  AIG78772.1
SOURCE      Amycolatopsis japonica
  ORGANISM  Amycolatopsis japonica
            Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
            Amycolatopsis; Amycolatopsis japonica group.
REFERENCE   1  (bases 1 to 8961318)
  AUTHORS   Stegmann,E., Albersmeier,A., Spohn,M., Gert,H., Weber,T.,
            Wohlleben,W., Kalinowski,J. and Ruckert,C.
  TITLE     Complete genome sequence of the actinobacterium Amycolatopsis
            japonica MG417-CF17(T) (=DSM 44213T) producing
            (S,S)-N,N'-ethylenediaminedisuccinic acid
  JOURNAL   J. Biotechnol. (2014) In press
   PUBMED   25193710
  REMARK    Publication Status: Available-Online prior to print
REFERENCE   2  (bases 1 to 8961318)
  AUTHORS   Ruckert,C., Stegmann,E., Spohn,M., Gert,H., Weber,T., Wohlleben,W.
            and Kalinowski,J.
  TITLE     Direct Submission
  JOURNAL   Submitted (17-JUL-2014) CeBiTec, Bielefeld University,
            Universitaetsstr. 27, Bielefeld, NRW 33615, Germany
COMMENT     ##Genome-Assembly-Data-START##
            Assembly Method       :: Newbler v. 2.5.3
            Genome Coverage       :: 23.56x
            Sequencing Technology :: 454
            ##Genome-Assembly-Data-END##
FEATURES             Qualifiers
     source          /organism="Amycolatopsis japonica"
                     /mol_type="genomic DNA"
                     /strain="MG417-CF17"
                     /isolation_source="soil"
                     /culture_collection="DSM:44213"
                     /type_material="type strain of Amycolatopsis japonica"
                     /db_xref="taxon:208439"
                     /country="Japan"
     protein         /gene="tig"
                     /locus_tag="AJAP_29700"
                     /EC_number="5.2.1.8"
                     /function="Involved in protein export. Acts as a chaperone
                     by maintaining the newly synthesized protein in an open
                     conformation. Functions as a peptidyl-prolyl cis-trans
                     isomerase (By similarity)."
                     /transl_table=11
BEGIN
        1 MKSTVEQLSP TRVKINVEVP FDELKPNFDR AYRKIAQQVR IPGFRPGKAP ARVLESRIGR
       61 APVLDEVVNE VIPAKYMEAV RAGEVRTLGQ PEFEVTKLED REVLEFTAEV DIRPEISLPD
      121 LEGFAVSVDD VELTDAEVDE QLDELRARFG TLTGVDRPAE NGDFVSIDLA ATVDGQEVEE
      181 ASTTGLSYEI GSGQLVDGID EAIIGANAGE TKTFTTKLVA GEHTGKDADV TVTVQTIKQR
      241 ELPEADDEFA QMASEFDTID ELKGDLRERL GRVKKMQQGV QARDKVLEEL LERTEVAIPE
      301 KVLEAEIENR KHDAIHPFDH DEAQFAKALE AEGRTIEEFD TEVREESEKA VRTQLLLDSI
      361 ADAEQTSVND GELTERIIYQ AQRFGVSPDE YVQRAQQSGQ LTAIYADVRR GKALASVVRK
      421 TTVTDASGAT VDLEELFGPA AEETQVTEET AKTAAE
//